Increasing stability and productivity of lipase enzyme by encapsulation in a porous organic-inorganic system

被引：74

作者：

Macario, Anastasia ^{[1
]}

Moliner, Manuel ^{[2
]}

Corma, Avelino ^{[2
]}

Giordano, Girolamo ^{[1
]}

机构：

[1] Univ Calabria, Dipartimento Ingn Chim & Mat, I-87036 Arcavacata Di Rende, CS, Italy

[2] Univ Politecn Valencia, Inst Tecnol Quim, CSIC, Valencia 46022, Spain

来源：

MICROPOROUS AND MESOPOROUS MATERIALS | 2009年 / 118卷 / 1-3期

关键词：

Sol-gel; Lipase; Encapsulation; Transesterification; Mesoporous materials; Biodiesel; SOL-GEL MATERIALS; MESOPOROUS MOLECULAR-SIEVES; PSEUDOMONAS-CEPACIA LIPASE; MUCOR-MIEHEI LIPASE; IMMOBILIZED LIPASE; SOYBEAN OIL; BIODIESEL PRODUCTION; COVALENT IMMOBILIZATION; AMORPHOUS ALPO4; ALKYL ESTER;

D O I：

10.1016/j.micromeso.2008.09.003

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

In this work, we report the encapsulation of lipase enzyme in highly ordered mesoporous matrix by a sol-gel method that involves the hydrolysis/polycondensation of a silica precursor at neutral pH and room temperature. The enzyme is encapsulated within the micellar phase of the surfactant that is self-assembled with silica. The encapsulated biocatalyst has been used for the transesterification reaction of triolein with methanol under solvent free conditions. The highest fatty acid methyl esters yield (77%) was obtained after 96 h at 40 degrees C, with triolein: methanol molar ratio equal to 1:3 and with a very low amount of enzyme. Total productivity of the immobilized enzyme is almost six times higher than the one obtained using free lipase. The results clearly indicate that the immobilization procedure of lipase preserves the mobility of the enzyme and allows to increase its stability. (C) 2008 Elsevier Inc. All rights reserved.

引用

页码：334 / 340

页数：7

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